ID B8P4M5_POSPM Unreviewed; 876 AA.
AC B8P4M5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EED84180.1};
GN ORFNames=POSPLDRAFT_94480 {ECO:0000313|EMBL:EED84180.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED84180.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155}.
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DR EMBL; EQ966254; EED84180.1; -; Genomic_DNA.
DR RefSeq; XP_002470642.1; XM_002470597.1.
DR AlphaFoldDB; B8P4M5; -.
DR STRING; 561896.B8P4M5; -.
DR KEGG; ppl:POSPLDRAFT_94480; -.
DR HOGENOM; CLU_014332_0_0_1; -.
DR InParanoid; B8P4M5; -.
DR OMA; PEQISTF; -.
DR OrthoDB; 5488626at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048723; PRS7-like_OB.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF13; 26S PROTEASOME REGULATORY SUBUNIT 7; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF21236; PRS7_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 238..377
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 682..869
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 710..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 96095 MW; 6F6CE64B8CFC5A66 CRC64;
MAPKSDWEKW EKKADDKDEK EIKGTLIYPL SLLDMLTEVQ PSTTGQGPYA QKLKKIENDI
KDAQKRVNEK LGIKESDTGL AAPNLWDLAV DRQRMGEEHP LQVARCTKII PMNQEAAAAA
RAVNPQGALQ GQKGADEQDK YVINIKQIAK FVVGLGDRVA PTDIEEGMRV GVDRNKYQIQ
IPLPPKIDAS VTMMQVEEKP DVTYSDVGGC KEQIEKLREV VETPLLSPER FVNLGIDPPK
GVLLFGPPGT GKTLCARAVA NRTDATFIRV IGSELVQKYV GEGARMVREL FEMARSKKAC
IIFFDEVDAI GGARFDDGAG GDNEVQRTML ELINQLDGFD PRGNIKVLMA TNRPDTLDPA
LLRPGRLDRR VEFSLPDVEG RASILRIHAR SMSCERDIRF DLIARLCPNT TGAELRSVAT
EAGMFAIRAR RKVATERDFL DAVEKVVRQG TKFSSTDYED GGISAAELSR LMEEHAEQPP
RPLTLSTLLS LADPVTPESV LTSVRYVTNE IPRRMAMRAR SLEALPYIVG MNPFIARTLE
AYRKSFRFLT TYPPVQTLED NQRLTAELDG LVQSHANDIP TMAKGFQECA RYLTPEQIST
FLDEAIRNRI AVRLIAEQHI AISRALEEGG DLKDHHGVVH LSCSPQDMIR MCGSWVSDLC
EATLGAHPEI IIDGEVDATF AYVPVHLEYI LTEILKNAFR ATVERHARQP SSIRTSPVPP
VRITISPPPL TPIPRPRFLS MRVRDQGGGV SPAHLAQIFS YSFTTAGRAT TSPGGGVGWD
DQETGGGPYA AQHVGGSAAI GGIDSMGGAG GLFAEMTGRG VQVGMGTIAG LGYGLPMSRL
YTRYFGGSLD LMSLDGWGCD VFLKLRCLDD AGDVEI
//
